2V0H
Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-01 |
Detector | ADSC CCD |
Spacegroup name | H 3 2 |
Unit cell lengths | 108.459, 108.459, 327.154 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 111.800 - 1.790 |
R-factor | 0.192 |
Rwork | 0.191 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hv9 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.001 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.840 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.050 | 0.310 |
Number of reflections | 67671 | |
<I/σ(I)> | 29 | 4 |
Completeness [%] | 95.1 | 74.8 |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 1.2-1.8M AMMONIUM SULFATE, 2% PEG-400, 0.1M MES PH 5.2 TO 6.5, AND COBALT (II) CHLORIDE 6.25 MM |